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Regulation of a rat VL30 element in human breast cancer cells in hypoxia and anoxia: role of HIF-1.

Ameri K, Burke B, Lewis CE, Harris AL - Br. J. Cancer (2002)

Bottom Line: Novel approaches to cancer gene therapy currently exploit tumour hypoxia to achieve transcriptional targeting using oxygen-regulated enhancer elements called hypoxia response elements.Mutational analysis demonstrated that the base immediately 5' to this modulates the anoxic/hypoxic induction of the secondary anoxia response element, such that TACGTG>GACGTG>CACGTG.A similar correlation was found for erythropoietin, phosphoglycerate kinase 1, and aldolase hypoxia response elements, which contain these respective 5' flanking bases.

View Article: PubMed Central - PubMed

Affiliation: Tumour Targeting Group, Division of Genomic Medicine, University of Sheffield Medical School, Beech Hill Road, Sheffield S10 2RX, UK.

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Related in: MedlinePlus

(a) Electrophoretic mobility supershift assay showing HIF-1 binding to wt SARE in nuclear extracts of MCF-7 cells exposed for 16 h to anoxia. The inducible HIF-1 band is super-shifted by addition of a monoclonal antibody to HIF-1α. Addition of the antibody to EPAS 1 (HIF-2α or ATF-1 failed to supershift the constitutive factors (‘C’) or the inducible band in anoxia. (b) Electrophoretic mobility supershift assay showing HIF-1 binding to wt SARE in nuclear extracts of MCF-7 cells exposed for 16 h to anoxia. The inducible HIF-1 band is super-shifted by addition of a monoclonal antibody to HIF-1α. M2 (which lacked the HBS) failed to bind the inducible HIF-1 in the assay conditions used.
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fig7: (a) Electrophoretic mobility supershift assay showing HIF-1 binding to wt SARE in nuclear extracts of MCF-7 cells exposed for 16 h to anoxia. The inducible HIF-1 band is super-shifted by addition of a monoclonal antibody to HIF-1α. Addition of the antibody to EPAS 1 (HIF-2α or ATF-1 failed to supershift the constitutive factors (‘C’) or the inducible band in anoxia. (b) Electrophoretic mobility supershift assay showing HIF-1 binding to wt SARE in nuclear extracts of MCF-7 cells exposed for 16 h to anoxia. The inducible HIF-1 band is super-shifted by addition of a monoclonal antibody to HIF-1α. M2 (which lacked the HBS) failed to bind the inducible HIF-1 in the assay conditions used.

Mentions: Antibodies to HIF-2α (EPAS 1), and ATF-1 did not supershift the complex bound to the SARE trimer (Figure 7aFigure 7


Regulation of a rat VL30 element in human breast cancer cells in hypoxia and anoxia: role of HIF-1.

Ameri K, Burke B, Lewis CE, Harris AL - Br. J. Cancer (2002)

(a) Electrophoretic mobility supershift assay showing HIF-1 binding to wt SARE in nuclear extracts of MCF-7 cells exposed for 16 h to anoxia. The inducible HIF-1 band is super-shifted by addition of a monoclonal antibody to HIF-1α. Addition of the antibody to EPAS 1 (HIF-2α or ATF-1 failed to supershift the constitutive factors (‘C’) or the inducible band in anoxia. (b) Electrophoretic mobility supershift assay showing HIF-1 binding to wt SARE in nuclear extracts of MCF-7 cells exposed for 16 h to anoxia. The inducible HIF-1 band is super-shifted by addition of a monoclonal antibody to HIF-1α. M2 (which lacked the HBS) failed to bind the inducible HIF-1 in the assay conditions used.
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Related In: Results  -  Collection

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getmorefigures.php?uid=PMC2376195&req=5

fig7: (a) Electrophoretic mobility supershift assay showing HIF-1 binding to wt SARE in nuclear extracts of MCF-7 cells exposed for 16 h to anoxia. The inducible HIF-1 band is super-shifted by addition of a monoclonal antibody to HIF-1α. Addition of the antibody to EPAS 1 (HIF-2α or ATF-1 failed to supershift the constitutive factors (‘C’) or the inducible band in anoxia. (b) Electrophoretic mobility supershift assay showing HIF-1 binding to wt SARE in nuclear extracts of MCF-7 cells exposed for 16 h to anoxia. The inducible HIF-1 band is super-shifted by addition of a monoclonal antibody to HIF-1α. M2 (which lacked the HBS) failed to bind the inducible HIF-1 in the assay conditions used.
Mentions: Antibodies to HIF-2α (EPAS 1), and ATF-1 did not supershift the complex bound to the SARE trimer (Figure 7aFigure 7

Bottom Line: Novel approaches to cancer gene therapy currently exploit tumour hypoxia to achieve transcriptional targeting using oxygen-regulated enhancer elements called hypoxia response elements.Mutational analysis demonstrated that the base immediately 5' to this modulates the anoxic/hypoxic induction of the secondary anoxia response element, such that TACGTG>GACGTG>CACGTG.A similar correlation was found for erythropoietin, phosphoglycerate kinase 1, and aldolase hypoxia response elements, which contain these respective 5' flanking bases.

View Article: PubMed Central - PubMed

Affiliation: Tumour Targeting Group, Division of Genomic Medicine, University of Sheffield Medical School, Beech Hill Road, Sheffield S10 2RX, UK.

Show MeSH
Related in: MedlinePlus